ZN431_MOUSE
ID ZN431_MOUSE Reviewed; 526 AA.
AC E9QAG8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Zinc finger protein 431;
DE AltName: Full=Zinc finger protein 932;
GN Name=Znf431; Synonyms=Zfp431, Zfp932;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH HDAC1 AND HDAC2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21177534; DOI=10.1074/jbc.m110.178780;
RA He Z., Cai J., Lim J.W., Kroll K., Ma L.;
RT "A novel KRAB domain-containing zinc finger transcription factor ZNF431
RT directly represses Patched1 transcription.";
RL J. Biol. Chem. 286:7279-7289(2011).
RN [4]
RP FUNCTION, INTERACTION WITH HDAC2, AND DEVELOPMENTAL STAGE.
RX PubMed=22391310; DOI=10.1016/b978-0-12-394622-5.00014-6;
RA Huang G.J., He Z., Ma L.;
RT "ZFP932 suppresses cellular Hedgehog response and Patched1 transcription.";
RL Vitam. Horm. 88:309-332(2012).
CC -!- FUNCTION: Sequence-specific DNA binding transcriptional repressor.
CC Represses target gene transcription by recruiting HDAC1 and HDAC2
CC histone deacetylases. Acts as a specific transcriptional repressor for
CC PTCH1 during embryonic development. Required for osteoblast
CC differentiation and sonic hedgehog/SHH signaling response. Binds to the
CC consensus site 5'-GCGCCC-3' in the promoter of PTCH1.
CC {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC -!- SUBUNIT: Interacts (via KRAB domain) with HDAC2; the interaction is
CC direct. Interacts (via KRAB domain) with HDAC1.
CC {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC -!- INTERACTION:
CC E9QAG8; O09106: Hdac1; NbExp=3; IntAct=EBI-9549639, EBI-301912;
CC E9QAG8; P70288: Hdac2; NbExp=3; IntAct=EBI-9549639, EBI-302251;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, thymus, spleen,
CC lymph node, liver, kidney, muscle, testis, ovary, skin and uterus.
CC {ECO:0000269|PubMed:21177534}.
CC -!- DEVELOPMENTAL STAGE: Expressed in limb mesenchyme at 10.5 dpc.
CC Expressed in tooth, submandibular glands, thymus, thyroid, vibrissa
CC follicles at 14.5 dpc. {ECO:0000269|PubMed:21177534,
CC ECO:0000269|PubMed:22391310}.
CC -!- DOMAIN: The KRAB domain is necessary for its repressive activity.
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DR EMBL; AC123679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012405; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS59681.1; -.
DR RefSeq; NP_663538.2; NM_145563.2.
DR AlphaFoldDB; E9QAG8; -.
DR SMR; E9QAG8; -.
DR BioGRID; 213490; 26.
DR IntAct; E9QAG8; 2.
DR STRING; 10090.ENSMUSP00000108159; -.
DR iPTMnet; E9QAG8; -.
DR PhosphoSitePlus; E9QAG8; -.
DR MaxQB; E9QAG8; -.
DR PaxDb; E9QAG8; -.
DR PRIDE; E9QAG8; -.
DR Ensembl; ENSMUST00000112540; ENSMUSP00000108159; ENSMUSG00000066613.
DR GeneID; 69504; -.
DR KEGG; mmu:69504; -.
DR UCSC; uc008ypn.1; mouse.
DR CTD; 69504; -.
DR MGI; MGI:1916754; Zfp932.
DR VEuPathDB; HostDB:ENSMUSG00000066613; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154469; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; E9QAG8; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; E9QAG8; -.
DR TreeFam; TF338854; -.
DR BioGRID-ORCS; 69504; 6 hits in 36 CRISPR screens.
DR ChiTaRS; Zfp932; mouse.
DR PRO; PR:E9QAG8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; E9QAG8; protein.
DR Bgee; ENSMUSG00000066613; Expressed in ovary and 99 other tissues.
DR ExpressionAtlas; E9QAG8; baseline and differential.
DR Genevisible; E9QAG8; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Differentiation; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..526
FT /note="Zinc finger protein 431"
FT /id="PRO_0000425265"
FT DOMAIN 5..76
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 104..126
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..154
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 160..182
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CONFLICT 323
FT /note="I -> T (in Ref. 2; BC012405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 61280 MW; 1F7F44631FEB1BA2 CRC64;
MVDALTYDDV YVNFTQEEWA LLNPSQKSLY KDVMLETYRN LNAVGYNWED SNIEEHCESS
RRHGRHERNH TGEKPYEGIQ YGEAFVHHSS LQMRKIIHTG EKRYKCNQCD KAYSRHSILQ
IHKRTHSGEK PYECNQCGKA FTQHSHLKIH MVTHTGEKPY KCDQCGKAFA FHSTLQVHKR
THTGEKPYEC NQCSKAFAHH CHLRVHKRIH TGEKPYKCDQ CGKAFVGQND LKRHERVHTG
EKPYKCNECG KAFVCNASLR THKTTHTGVK PYECKQCTKS FASHGQLQKH ERIHTGEKPY
KCDQCGKAFA SHDKFQKHER IHIGEKPYKC KQCTKSFASH DKLQKHERIH TGEKPYECKQ
CTKSFASHNK LQKHERIHTG EKPYKCDQCN KAFVYESYLQ VHKKTHTGEK PYKCNECGKA
FARHSHLKVH KITHTGEKPY KCNQCGKALA YHSTLQVHQR THTGEKPYEC EQCGKAFANQ
SYFQVHKRIH TGEKPYKCDQ CGKAFVGSSD LKRHERVHTG RETLQM
